A fearsome health calamity- the novel coronavirus of 2019 struck the world and created havoc with its rapid spread. Various countries got affected in terms of economic and other losses and the extent of impact depended on the pre-existing financial arrangement of the country and various other factors. Due to this outbreak, healthcare sector was one of the worst affected. Also, it needed most investment and had to respond quickly and effectively to manage this crisis. Among the countries affected, India- a financial centre with significant worldwide connectivity was impacted directly, leading to an imminent breakdown of economical markets. This paper tries to understand the different aspects of economic challenges faced by the Indian healthcare system and devise the possible measures to overcome the effect of COVID-19 pandemic in India. It analyses the short term and possible long-term impact of this pandemic on the health care sector of India in terms of efficiency and equity. The Indian Government had acted rapidly to allocate funds, resources and manpower. It announced relief packages for the marginalized communities and covered costs. Specific research centres in the country need to work to quickly mitigate any further damage.

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Large-scale interdomain rearrangements are essential to protein function, governing the activity of large enzymes and molecular machineries. Yet, obtaining an atomic-resolution understanding of how the relative domain positioning is affected by external stimuli is a hard task in modern structural biology. Here, we show that combining structural modeling by AlphaFold2 with coarse-grained molecular dynamics simulations and NMR residual dipolar coupling data is sufficient to characterize the spatial domain organization of bacterial enzyme I (EI), a ∼130 kDa multidomain oligomeric protein that undergoes large-scale conformational changes during its catalytic cycle. In particular, we solve conformational ensembles for EI at two different experimental temperatures and demonstrate that a lower temperature favors sampling of the catalytically competent closed state of the enzyme. These results suggest a role for conformational entropy in the activation of EI and demonstrate the ability of our protocol to detect and characterize the effect of external stimuli (such as mutations, ligand binding, and post-translational modifications) on the interdomain organization of multidomain proteins. We expect the ensemble refinement protocol described here to be easily transferrable to the investigation of the structure and dynamics of other uncharted multidomain systems and have assembled a Google Colab page () to facilitate implementation of the presented methodology elsewhere.

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